1i3z
From Proteopedia
(New page: 200px<br /><applet load="1i3z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i3z, resolution 2.15Å" /> '''MURINE EAT2 SH2 DOMA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1i3z.gif|left|200px]]<br /><applet load="1i3z" size=" | + | [[Image:1i3z.gif|left|200px]]<br /><applet load="1i3z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i3z, resolution 2.15Å" /> | caption="1i3z, resolution 2.15Å" /> | ||
'''MURINE EAT2 SH2 DOMAIN IN COMPLEX WITH SLAM PHOSPHOPEPTIDE'''<br /> | '''MURINE EAT2 SH2 DOMAIN IN COMPLEX WITH SLAM PHOSPHOPEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The T and natural killer (NK) cell-specific gene SAP (SH2D1A) encodes a | + | The T and natural killer (NK) cell-specific gene SAP (SH2D1A) encodes a 'free SH2 domain' that binds a specific tyrosine motif in the cytoplasmic tail of SLAM (CD150) and related cell surface proteins. Mutations in SH2D1A cause the X-linked lymphoproliferative disease, a primary immunodeficiency. Here we report that a second gene encoding a free SH2 domain, EAT-2, is expressed in macrophages and B lympho cytes. The EAT-2 structure in complex with a phosphotyrosine peptide containing a sequence motif with Tyr281 of the cytoplasmic tail of CD150 is very similar to the structure of SH2D1A complexed with the same peptide. This explains the high affinity of EAT-2 for the pTyr motif in the cytoplasmic tail of CD150 but, unlike SH2D1A, EAT-2 does not bind to non-phosphorylated CD150. EAT-2 binds to the phosphorylated receptors CD84, CD150, CD229 and CD244, and acts as a natural inhibitor, which interferes with the recruitment of the tyrosine phosphatase SHP-2. We conclude that EAT-2 plays a role in controlling signal transduction through at least four receptors expressed on the surface of professional antigen-presenting cells. |
==About this Structure== | ==About this Structure== | ||
| - | 1I3Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1I3Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3Z OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Eck, M | + | [[Category: Eck, M J.]] |
[[Category: Lu, J.]] | [[Category: Lu, J.]] | ||
[[Category: Morra, M.]] | [[Category: Morra, M.]] | ||
| Line 20: | Line 20: | ||
[[Category: sh2 domain phosphotyrosine signal transduction lymphocyte]] | [[Category: sh2 domain phosphotyrosine signal transduction lymphocyte]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:45 2008'' |
Revision as of 11:07, 21 February 2008
|
MURINE EAT2 SH2 DOMAIN IN COMPLEX WITH SLAM PHOSPHOPEPTIDE
Overview
The T and natural killer (NK) cell-specific gene SAP (SH2D1A) encodes a 'free SH2 domain' that binds a specific tyrosine motif in the cytoplasmic tail of SLAM (CD150) and related cell surface proteins. Mutations in SH2D1A cause the X-linked lymphoproliferative disease, a primary immunodeficiency. Here we report that a second gene encoding a free SH2 domain, EAT-2, is expressed in macrophages and B lympho cytes. The EAT-2 structure in complex with a phosphotyrosine peptide containing a sequence motif with Tyr281 of the cytoplasmic tail of CD150 is very similar to the structure of SH2D1A complexed with the same peptide. This explains the high affinity of EAT-2 for the pTyr motif in the cytoplasmic tail of CD150 but, unlike SH2D1A, EAT-2 does not bind to non-phosphorylated CD150. EAT-2 binds to the phosphorylated receptors CD84, CD150, CD229 and CD244, and acts as a natural inhibitor, which interferes with the recruitment of the tyrosine phosphatase SHP-2. We conclude that EAT-2 plays a role in controlling signal transduction through at least four receptors expressed on the surface of professional antigen-presenting cells.
About this Structure
1I3Z is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells., Morra M, Lu J, Poy F, Martin M, Sayos J, Calpe S, Gullo C, Howie D, Rietdijk S, Thompson A, Coyle AJ, Denny C, Yaffe MB, Engel P, Eck MJ, Terhorst C, EMBO J. 2001 Nov 1;20(21):5840-52. PMID:11689425
Page seeded by OCA on Thu Feb 21 13:07:45 2008
